Peas (the seed from the Pisum Sativum plant) is an important source of protein for humans and animals, both in its unprocessed and processed form.
WO 2011/122937, WO 1998/033388 and WO 2011/050471 all concern various aspects of isolating, purifying and using pea protein. In addition, Croy et al. Biochem J. 1980, 191, 509-516 discusses the purification and characterisation of convicilin from peas.
Previous processes for isolating pea protein fractions have typically involved precipitation of given fractions. In salt fractionations, legumin precipitates in salt, and vicilin remains soluble. However, convicilin has proved to be a contaminant, and is difficult to avoid when isolating a vicilin-rich fraction. Legumin fractions are also often contaminated with convicilin. Convicilin contamination is typical in large-scale isolation processes (see e.g. Geuguen et al. J. Sci. Food Agric. 1984, 35, 1024-1033; Lame & Gueguen, J. Chromatogr. 1986, 361, 169-178).